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Article

Purification and biochemical characterization of recombinant alpha 1-antitrypsin variants expressed in Escherichia coli.

Biochemistry - 9 Apr 1991

Bischoff R, Speck D, Lepage P, Delatre L, Ledoux C, Brown S W, Roitsch C

Abstract excerpt

Site-directed variants of alpha 1-antitrypsin (alpha 1AT) expressed in a recombinant strain of Escherichia coli have been isolated with an overall process yield of 50% following tangential flow ultrafiltration, anion-exchange, immobilized metal affinity, and hydrophobic interaction chromatography. The primary structure of the purified variants including the integrity of the N- and C-termini has been verified by...

Topics

Amino Acid Sequence
Autoanalysis
Chromatography, Gel
Chromatography, High Pressure Liquid
Endotoxins
Escherichia coli
Gene Expression
Genetic Variation
Isoelectric Focusing
Mass Spectrometry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Peptide Mapping

Recombinant Proteins

alpha 1-Antitrypsin

Source

Identifiers

PMID: 2012806
DOI: 10.1021/bi00228a017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2012806-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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